Crystal structure of human UP1, the domain of hnRNP A1 that contains two RNA-recognition motifs
- 1 April 1997
- Vol. 5 (4) , 559-570
- https://doi.org/10.1016/s0969-2126(97)00211-6
Abstract
No abstract availableKeywords
This publication has 61 references indexed in Scilit:
- hnRNP A1 Selectively Interacts Through its Gly-rich Domain with Different RNA-binding ProteinsJournal of Molecular Biology, 1996
- Specificity of ribonucleoprotein interaction determined by RNA folding during complex formationNature, 1996
- Origins of Binding Specificity of the A1 Heterogeneous Nuclear RibonucleoproteinBiochemistry, 1996
- Both RNA-Binding Domains in Heterogeneous Nuclear Ribonucleoprotein A1 Contribute Toward Single-Stranded-RNA BindingBiochemistry, 1994
- hnRNP PROTEINS AND THE BIOGENESIS OF mRNAAnnual Review of Biochemistry, 1993
- Mammalian Heterogeneous Ribonucleoprotein A1 and its Constituent Domains: Nucleic Acid Interaction, Structural Stability and Self-associationJournal of Molecular Biology, 1993
- Proton, carbon-13, and nitrogen-15 NMR assignments and global folding pattern of the RNA-binding domain of the human hnRNP C proteinsBiochemistry, 1992
- Shuttling of pre-mRNA binding proteins between nucleus and cytoplasmNature, 1992
- Interactions of the A1 heterogeneous nuclear ribonucleoprotein and its proteolytic derivative, UP1, with RNA and DNA: Evidence for multiple RNA binding domains and salt-dependent binding mode transitionsBiochemistry, 1991
- Studies of the strand-annealing activity of mammalian hnRNP complex protein A1Biochemistry, 1990